Structural stability from solution to the gas phase: native solution structure of ubiquitin survives analysis in a solvent-free ion mobility-mass spectrometry environment.
about
Native Mass Spectrometry in Fragment-Based Drug DiscoveryFactors That Drive Peptide Assembly from Native to Amyloid Structures: Experimental and Theoretical Analysis of [Leu-5]-Enkephalin MutantsRobotically assisted titration coupled to ion mobility-mass spectrometry reveals the interface structures and analysis parameters critical for multiprotein topology mappingNative electrospray ionization and electron-capture dissociation for comparison of protein structure in solution and the gas phase.Collisional and Coulombic unfolding of gas-phase proteins: high correlation to their domain structures in solution.Conformational changes of ubiquitin during electrospray ionization as determined by in-ESI source H/D exchange combined with high-resolution MS and ECD fragmentation.Solvent-induced structural transitions of lysozyme in an electrospray ionization source.Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues.Gas-phase protein conformation/multimer ion formation by electrospray ion mobility-mass spectrometry: bovine insulin and ubiquitin.Effects of Fe(II)/H2O2 oxidation on ubiquitin conformers measured by ion mobility-mass spectrometry.Gas-phase intramolecular protein crosslinking via ion/ion reactions: ubiquitin and a homobifunctional sulfo-NHS esterNative-Like and Denatured Cytochrome c Ions Yield Cation-to-Anion Proton Transfer Reaction Products with Similar Collision Cross-Sections.The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes.Large-scale collision cross-section profiling on a traveling wave ion mobility mass spectrometer.Tandem ion mobility spectrometry coupled to laser excitation.How ubiquitin unfolds after transfer into the gas phase.Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.New supercharging reagents produce highly charged protein ions in native mass spectrometry.Isolating Protein Charge State Reduction in Electrospray Droplets Using Femtosecond Laser Vaporization.Probing Asymmetric Charge Partitioning of Protein Oligomers during Tandem Mass Spectrometry.Parallel β-sheet vibrational couplings revealed by 2D IR spectroscopy of an isotopically labeled macrocycle: quantitative benchmark for the interpretation of amyloid and protein infrared spectra.Hofmeister salts recover a misfolded multiprotein complex for subsequent structural measurements in the gas phaseRetention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study.Exploring salt bridge structures of gas-phase protein ions using multiple stages of electron transfer and collision induced dissociation.Mass spectrometry based tools to investigate protein-ligand interactions for drug discovery.Advances in ion mobility-mass spectrometry instrumentation and techniques for characterizing structural heterogeneity.Charge-Induced Unzipping of Isolated Proteins to a Defined Secondary Structure.Evidence for two new solution states of ubiquitin by IMS-MS analysis.Comprehensive Gas-Phase Peptide Ion Structure Studies Using Ion Mobility Techniques: Part 2. Gas-Phase Hydrogen/Deuterium Exchange for Ion Population Estimation.Molecular Structures and Momentum Transfer Cross Sections: The Influence of the Analyte Charge Distribution.Comprehensive Peptide Ion Structure Studies Using Ion Mobility Techniques: Part 1. An Advanced Protocol for Molecular Dynamics Simulations and Collision Cross-Section Calculation.Top-Down Mass Spectrometry: Proteomics to Proteoforms.Chemical Probes and Engineered Constructs Reveal a Detailed Unfolding Mechanism for a Solvent-Free Multidomain Protein.Combining ion mobility spectrometry with hydrogen-deuterium exchange and top-down MS for peptide ion structure analysis.Determination of ion mobility collision cross sections for unresolved isomeric mixtures using tandem mass spectrometry and chemometric deconvolution.Action-FRET of a Gaseous ProteinGas-phase microsolvation of ubiquitin: investigation of crown ether complexation sites using ion mobility-mass spectrometryAnalyzing slowly exchanging protein conformations by ion mobility mass spectrometry: study of the dynamic equilibrium of prolyl oligopeptidase.Early stages of insulin fibrillogenesis examined with ion mobility mass spectrometry and molecular modelling.Microheterogeneity within conformational states of ubiquitin revealed by high resolution trapped ion mobility spectrometry.
P2860
Q26740022-801772E7-D709-450C-BDC9-C751453091BEQ27684284-AD4B8137-0096-49E8-B011-29AE979EDA06Q30354958-CF1ACEB3-310A-4064-A660-13DC9B7D5EA5Q30357152-EAE706B9-A7E4-4595-9FD6-40A2F202A1C2Q30364286-67D69029-D3B4-4968-9E29-93B51F817FFFQ30367701-D461D248-1DD7-43DA-8953-BC2F814E933BQ30373499-103B8DF0-2EB0-462F-B8DE-1B8367751794Q30379165-F2A0E94E-14D1-4B4D-B0A0-A933163FB201Q30393122-059345FC-9292-4368-96DB-89949B40D602Q30424397-9F7CDDB9-FBEE-461A-ADE7-63E96196884EQ30427890-255CA759-4747-4089-AF5E-A738DAACE763Q33469866-ABECE6E7-B322-4716-AE02-832006EAA7C3Q34357280-2C5B7908-7426-41BB-A1C5-AC76FBCAD32DQ34474082-2B489F59-F788-4599-865B-A710D066940BQ35796203-375D00CD-2151-496E-80FE-61484EBA6B61Q35936223-987375D6-8DBB-43C2-A79E-5E5980F68724Q36198935-BF449CF9-A30E-49B8-BACA-65302740F2EAQ36199100-5E2C8AD9-7BD3-467D-B7A5-E213F0A9D06DQ36243621-2E104F2E-1ED5-4F0F-AA88-78C22BBFD0FCQ36357695-A1F936B5-528B-4ABE-85F0-66AA5929B041Q36469264-ED80E7E9-C304-4878-9D28-025DCB5CF03CQ37202930-A1F1E0CC-D64F-451F-BAA5-818AE1FA57E0Q37420549-89D1B74B-2C28-4362-B1DA-DD5C2EEB39BAQ37658516-81471075-3E97-4225-8189-7BB4B6B4F335Q38005330-11B2A6DA-54D1-4768-8BD0-70C1377EFC6FQ38538398-0F24134A-0E81-45EB-AEE1-BD46F26EA391Q38670301-8D47706F-F6ED-4BEE-BBF9-D99CF973F2C4Q38706259-9795BDB3-F18B-4FD6-B037-1BE074D38A88Q38896696-5792BBBD-5C4C-4A18-95BE-E980A3F654A3Q38934268-173F54EB-C16E-4DC3-AD66-5EDE7F1A32D8Q38955798-26144D3E-34AB-4122-BEAC-B949C6E6F72EQ39038792-7A7C34B2-A689-40C5-AFFD-C701BD1B942DQ39105512-0C2041E0-6F42-4AC8-86EE-BDC342AF238CQ39121316-7E942E4E-CA31-4D21-93D8-2699AC9B6695Q39379049-D533C503-572C-400A-9CB3-A09C398368DFQ39507281-96A4E11D-2D8C-409D-9EC4-BC009C3BEF97Q39521209-E49DB2EE-3DA0-43C2-AAAA-DD035D7B4EAFQ39584678-83871CF3-D844-48D5-AB3C-9A2BA41FE4C9Q40540564-7E109CF5-F7B9-4D8D-B9AE-65C7B013B373Q40803054-C6819336-D020-46C4-97E5-AC04A6F3D48C
P2860
Structural stability from solution to the gas phase: native solution structure of ubiquitin survives analysis in a solvent-free ion mobility-mass spectrometry environment.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Structural stability from solu ...... mass spectrometry environment.
@en
Structural stability from solu ...... mass spectrometry environment.
@nl
type
label
Structural stability from solu ...... mass spectrometry environment.
@en
Structural stability from solu ...... mass spectrometry environment.
@nl
prefLabel
Structural stability from solu ...... mass spectrometry environment.
@en
Structural stability from solu ...... mass spectrometry environment.
@nl
P356
P1476
Structural stability from solu ...... mass spectrometry environment.
@en
P2093
Michael T Bowers
Thomas Wyttenbach
P304
12266-12275
P356
10.1021/JP206867A
P407
P577
2011-09-30T00:00:00Z